Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Research Article
  • Published:

Inhibition of a starch-granule–bound protein leads to modified starch and repression of cold sweetening

Abstract

We have cloned a gene involved in starch metabolism that was identified by the ability of its product to bind to potato starch granules. Reduction in the protein level of transgenic potatoes leads to a reduction in the phosphate content of the starch. The complementary result is obtained when the protein is expressed in Escherichia coli, as this leads to an increased phosphate content of the glycogen. It is possible that this protein is responsible for the incorporation of phosphate into starch-like glucans, a process that is not understood at the biochemical level. The reduced phosphate content in potato starch has some secondary effects on its degradability, as the respective plants show a starch excess phenotype in leaves and a reduction in cold-sweetening in tubers.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Smith, A.M., Denyer, K., and Martin, C. 1997. The synthesis of the starch granule. Annual Review of Plant Physiology and Plant Molecular Biology 48: 67–87.

    Article  CAS  Google Scholar 

  2. Ball, S., Guan, H.-P., James, M. Myers, A., Keeling, P., Mouille, G., et al. 1996. From glycogen to amylopectin: a model explaining the biogenesis of the plant starch granule. Cell 86: 349–352.

    Article  CAS  Google Scholar 

  3. Jane, J., Kasemsuwan, T., Chen, J.F., and Juliano, B.O. 1996. Phosphorus in rice and other starches. Cereal Foods World 41: 827–832.

    CAS  Google Scholar 

  4. Robinson, K.A. and Schreier, H.J. 1994. Isolation, sequence and characterization of the maltose-regulated mlrA gene from the hyperthermophilic archaeum Pyrococcus furiosus. Gene 151: 173–176.

    Article  CAS  Google Scholar 

  5. Bay-Smidt, A.M., Wischmann, B.,, Olsen, C.E. and Nielsen, T.H. 1994. Starch bound phosphate in potato as studied by a simple method for determination of organic phosphate and 31P-NMR. Starch/Stärke 46: 167–172.

    CAS  Google Scholar 

  6. Swinkels, J.J.M. 1985. Composition and properties of commercial native starches. Starch/Stärke 37:1–5.

    Article  CAS  Google Scholar 

  7. Duwenig, E. Untersuchungen zur Funktion von α-1,4-Glucan-Phosphorylasen in höheren Pflanzen. (PhD thesis, University Potsdam, Germany, 1996).

  8. Ho, L.C. 1988. Metabolism and compartmentation of imported sugars in sink organs in relation to sink strength. Annual Review of Plant Physiology and Plant Molecular Biology 39:355–378.

    Article  CAS  Google Scholar 

  9. Trethewey, R.N. and ap Rees, T. 1994. A mutant of Arabidopsis thaliana lacking the ability to transport glucose across the chloroplast envelope. Biochem. J. 301: 449–454.

    Article  CAS  Google Scholar 

  10. Müller-Thurgau, H., 1882. Ueber Zuckeranhäufung in Pflanzenteilen in Folge Niederer Temperatur. Landwirtschaftliche Jahrbücher 11: 751–828.

    Google Scholar 

  11. Kossmann, J., Visser, R.G.F., Müller-Röber, B., Willmitzer, L., and Sonnewald, U. 1991. Cloning and expression analysis of a potato cDNA that encodes branching enzyme: evidence for co-expression of starch biosynthetic genes. Mol. Gen. Genet. 230:39–44.

    Article  CAS  Google Scholar 

  12. Höfgen, R. and Willmitzer, L. 1990. Biochemical and genetic analysis of different patatin isoforms expressed in various organs of potato (Solanum tuberosum L.). Plant Sci. 66:221–230.

    Article  Google Scholar 

  13. Rocha-Sosa, M., Sonnewald, U., Frommer, W., Stratmann, M., Schell, J., and Willmitzer, L. 1989. Both developmental and metabolic signals activate the promoter of the class I patatin gene. EMBO J. 8: 23–29.

    Article  CAS  Google Scholar 

  14. Logemann, J., Schell, J., and Willmitzer, L. 1987. Improved method for the isolation of RNA from plant tissue. Anal. Biochem. 163:16–20.

    Article  CAS  Google Scholar 

  15. Lehrach, H., Diamond, D., Wozney, J.M. and Boedtker, H. 1977. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry 16: 4743–4751.

    Article  CAS  Google Scholar 

  16. Amasino, R.M. 1986. Acceleration of nucleic acid hybridization rate by polyethylene glycol. Anal. Biochem. 152: 304–307.

    Article  CAS  Google Scholar 

  17. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.

    Article  CAS  Google Scholar 

  18. Müller-Röber, B.T., Kossmann, J., Hannah, L.C., Willmitzer, L., and Sonnewald, U. 1990. One of two different ADP-glucose pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose. Mol. Gen. Genet. 224:136–146.

    Article  Google Scholar 

  19. Nielsen, T.H., Wischmann, B., Enevoldsen, K., and Møller, B.L. 1994. Starch phosphorylation in potato tuber proceeds concurrently with de novo biosynthesis of starch. Plant Physiol. 105: 111–117.

    Article  CAS  Google Scholar 

  20. Ames, B.N. 1966. Assay of inorganic phosphate, total phosphate and phos-phatases. Methods Enzymol. 8: 115–118.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Jens Kossmann.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lorberth, R., Ritte, G., Willmitzer, L. et al. Inhibition of a starch-granule–bound protein leads to modified starch and repression of cold sweetening. Nat Biotechnol 16, 473–477 (1998). https://doi.org/10.1038/nbt0598-473

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nbt0598-473

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing